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Database: UniProt
Entry: A0A0E0GPA5_ORYNI
LinkDB: A0A0E0GPA5_ORYNI
Original site: A0A0E0GPA5_ORYNI 
ID   A0A0E0GPA5_ORYNI        Unreviewed;      1559 AA.
AC   A0A0E0GPA5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA03G23710.1};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA03G23710.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G23710.1};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA03G23710.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA03G23710.1};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   STRING; 4536.A0A0E0GPA5; -.
DR   EnsemblPlants; ONIVA03G23710.1; ONIVA03G23710.1; ONIVA03G23710.
DR   Gramene; ONIVA03G23710.1; ONIVA03G23710.1; ONIVA03G23710.
DR   eggNOG; ENOG502QQEW; Eukaryota.
DR   HOGENOM; CLU_246028_0_0_1; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR   CDD; cd01098; PAN_AP_plant; 2.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47976; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD2-5; 1.
DR   PANTHER; PTHR47976:SF117; G-TYPE LECTIN S-RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE LECRK4; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00108; B_lectin; 2.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS50927; BULB_LECTIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1559
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002360803"
FT   DOMAIN          17..150
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          514..790
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          814..944
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          1264..1535
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1213..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         545
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1559 AA;  174253 MW;  92F612DD83AF3685 CRC64;
     MAPPLFLLSL QLLVLLSSPS AQAQNISLGT SLTTQGPNNA WLSPSGDFAF GFRPIDGNSS
     FYLLAIWFNK ISDKTATWYA KTSEQEPQPI QVPSGSILQF TSTGVLSLRD PTNREVWNPG
     ATGAPYASML DTGNFVIAAA GGSTISWETF KNPTDTILVT QALSPGMKLR SRLLTTDYSN
     GRFLLNMETQ RAALYTMAVP SGNLYDPYWS TPIDENVTNQ VTNLVFNTTG RIYVSMKNGT
     QFNMTSGVIR SMEDYYHRAT LDPDGVFRQY VYPKKPSSMS QAWTAVSIQP ENICNAQTKV
     GSGTCGFNSY CMFDGSNNQT SCVCPEQYSF FDEVRKYRGC RPDFELQSCD LDEAASMAQY
     EFNLVNNVDW PQADYEWYTP IDMDECRRLC LIDCFCAVAV FHENTCWKKK LPLSNGIMGS
     GVQRTVLIKV PKSNSSQPEL RKSRKWKSDK KLWILGSSLL LGGSVIANFA LSSVLLFGTY
     CTITRKDVQP LQPSRDPGLP LKAFSYAELE KATDGFKEVL GTGASSIVYK GQLQDELGTY
     IAVKKIDKIQ HETEKEFAVE VQTIGRTYHK NLVRMLGFCN EGTERLLVYE FMVNGSLNRF
     LFSGVRPLWS LRVQLALGVA RGLLYLHEEC STQIIHCDIK PQNILLDDNF IAKISDFGLA
     KLLRTNQTQT YTGIRGTRGY VAPEWFKNVG ITAKVDVYSF GVILLELICC RQNVEMEAAE
     EEQSILTYWA NDCYRCGRVD LLVDGDDEAK LNIKKVERFV AVALWCLQEE PTMRPSILKV
     TQMLDGADAI PTPPDSSSVV NSTSKRLINS NGSSPVLAHP ATLATILHEI CPSSAKHQYR
     LLFDTPGDGN SSSYLLAVWF NKIADKTVVW YARTSSNGKD DTIPVQVQSG SVLKLADGAL
     SLRDPSGNEV WNPQVTDVGY ARMLDTGNFR LLGTDGATKW ESFGDPSDTI LPTQVLSLGT
     ALHSRLLATD YSNGRFQLKV QRDGNLVMYP DAVPSGYLYD PYWASNTVDN GSQLVNITSA
     GVDSMGDFFH RATLDTDGVF RQYVYPKNIH ARPLWPEQWT AVDVLPENIC QSIQTMVGSG
     ACGFNSYCTI DGTKNTTSCL CPQNYKFIDD KRKYKGCRPD FEPQNCDLDE TTAMLQYDMA
     PIDRVDWPLS DYEQYNPIDQ TECRRLCVID CFCAVAVFDK ASSTCWKKRF PLSNGKMDVN
     VPRTVLIKVP RSTNSPSVFS SGSSKWKEDK NITSRKKIQL SQPSNKSGLP PKIFTYSELE
     KATGGFQEVL GTGASGVVYK GQLQDEFGTN IAVKKIEKLQ QEAQKEFLVE VQTIGQTFHR
     NLVRLLGFCN EGTERLLVYE FMSNGSLNTF LFSDTHPHWS LRVQVALGVA RGLLYLHEEC
     NKQIIHCDMK PQNILLDDNF AAKISDFGLA KLLPVNQTQT NTGIRGTRGY VAPEWFKNIG
     ITSKVDVYSF GVILLELVCC RKNVELEVLD EEQTILTYWA NDCYKCGRID LLVAGDDEAI
     FNIKKVERFV AVALWCLQEE PSMRPTMLKS SMEVIKTNRC RSPRAISFVV IKYEQKVDQ
//
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